ID DJC14_HUMAN Reviewed; 702 AA. AC Q6Y2X3; A5YM67; Q17RY2; Q66K17; Q96N59; Q96T63; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 28-JAN-2026, entry version 166. DE RecName: Full=DnaJ homolog subfamily C member 14; DE AltName: Full=DnaJ protein homolog 3; DE AltName: Full=Dopamine receptor-interacting protein of 78 kDa; DE Short=DRIP78; DE AltName: Full=Human DnaJ protein 3; DE Short=hDj-3; GN Name=DNAJC14; Synonyms=DRIP78, HDJ3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=12768437; DOI=10.1007/s10038-003-0012-8; RA Chen J., Huang Y., Wu H., Ni X., Cheng H., Fan J., Gu S., Gu X., Cao G., RA Ying K., Mao Y., Lu Y., Xie Y.; RT "Molecular cloning and characterization of a novel human J-domain protein RT gene (HDJ3) from the fetal brain."; RL J. Hum. Genet. 48:217-221(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-702. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 490-702. RX PubMed=11331877; DOI=10.1038/35074561; RA Bermak J.C., Li M., Bullock C.M., Zhou Q.-Y.; RT "Regulation of transport of the dopamine D1 receptor by a new membrane- RT associated ER protein."; RL Nat. Cell Biol. 3:492-498(2001). CC -!- FUNCTION: Regulates the export of target proteins, such as DRD1, from CC the endoplasmic reticulum to the cell surface. {ECO:0000250}. CC -!- SUBUNIT: Interacts with the FxxxFxxxF motif of DRD1 via its C-terminal CC domain. {ECO:0000250}. CC -!- INTERACTION: CC Q6Y2X3; P82979: SARNP; NbExp=3; IntAct=EBI-10038974, EBI-347495; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Multi-pass membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and selectively CC expressed in brain, lung, liver, skeletal muscle and kidney. CC {ECO:0000269|PubMed:12768437}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71050.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY188447; AAO73451.1; -; mRNA. DR EMBL; EF560741; ABQ59051.1; -; mRNA. DR EMBL; CH471054; EAW96833.1; -; Genomic_DNA. DR EMBL; BC080655; AAH80655.1; -; mRNA. DR EMBL; BC117146; AAI17147.1; -; mRNA. DR EMBL; BC117148; AAI17149.1; -; mRNA. DR EMBL; AK055945; BAB71050.1; ALT_INIT; mRNA. DR EMBL; AF351784; AAK56241.1; -; mRNA. DR CCDS; CCDS8894.1; -. DR RefSeq; NP_001381616.1; NM_001394687.1. DR RefSeq; NP_001381617.1; NM_001394688.1. DR RefSeq; NP_001381618.1; NM_001394689.1. DR RefSeq; NP_115740.5; NM_032364.5. DR AlphaFoldDB; Q6Y2X3; -. DR SMR; Q6Y2X3; -. DR BioGRID; 124515; 53. DR CORUM; Q6Y2X3; -. DR FunCoup; Q6Y2X3; 700. DR IntAct; Q6Y2X3; 13. DR MINT; Q6Y2X3; -. DR STRING; 9606.ENSP00000350223; -. DR GlyCosmos; Q6Y2X3; 1 site, 1 glycan. DR GlyGen; Q6Y2X3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6Y2X3; -. DR PhosphoSitePlus; Q6Y2X3; -. DR BioMuta; DNAJC14; -. DR DMDM; 110808200; -. DR jPOST; Q6Y2X3; -. DR MassIVE; Q6Y2X3; -. DR PaxDb; 9606-ENSP00000350223; -. DR PeptideAtlas; Q6Y2X3; -. DR ProteomicsDB; 67835; -. DR Pumba; Q6Y2X3; -. DR Antibodypedia; 3011; 61 antibodies from 14 providers. DR DNASU; 85406; -. DR Ensembl; ENST00000317287.5; ENSP00000317500.5; ENSG00000135392.20. DR Ensembl; ENST00000357606.7; ENSP00000350223.3; ENSG00000135392.20. DR Ensembl; ENST00000546957.2; ENSP00000448876.2; ENSG00000135392.20. DR Ensembl; ENST00000547445.2; ENSP00000450196.2; ENSG00000135392.20. DR Ensembl; ENST00000678005.2; ENSP00000504134.1; ENSG00000135392.20. DR GeneID; 85406; -. DR KEGG; hsa:85406; -. DR MANE-Select; ENST00000678005.2; ENSP00000504134.1; NM_032364.6; NP_115740.5. DR UCSC; uc001shx.1; human. DR AGR; HGNC:24581; -. DR ClinPGx; PA134940402; -. DR CTD; 85406; -. DR DisGeNET; 85406; -. DR GeneCards; DNAJC14; -. DR HGNC; HGNC:24581; DNAJC14. DR HPA; ENSG00000135392; Low tissue specificity. DR MIM; 606092; gene. DR OpenTargets; ENSG00000135392; -. DR VEuPathDB; HostDB:ENSG00000135392; -. DR eggNOG; KOG0720; Eukaryota. DR GeneTree; ENSGT00940000155637; -. DR HOGENOM; CLU_020746_0_0_1; -. DR InParanoid; Q6Y2X3; -. DR OMA; WLELPWF; -. DR OrthoDB; 1507364at2759; -. DR PAN-GO; Q6Y2X3; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q6Y2X3; -. DR PathwayCommons; Q6Y2X3; -. DR SignaLink; Q6Y2X3; -. DR SIGNOR; Q6Y2X3; -. DR Agora; ENSG00000135392; -. DR BioGRID-ORCS; 85406; 13 hits in 1155 CRISPR screens. DR ChiTaRS; DNAJC14; human. DR GeneWiki; DNAJC14; -. DR GenomeRNAi; 85406; -. DR Pharos; Q6Y2X3; Tbio. DR PRO; PR:Q6Y2X3; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q6Y2X3; protein. DR Bgee; ENSG00000135392; Expressed in islet of Langerhans and 147 other cell types or tissues. DR ExpressionAtlas; Q6Y2X3; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0050780; F:dopamine receptor binding; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd06257; DnaJ; 1. DR FunFam; 1.10.287.110:FF:000057; dnaJ homolog subfamily C member 14; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR032843; Jiv. DR InterPro; IPR052317; Viral_replicn-host_int_reg. DR PANTHER; PTHR44665; DNAJ HOMOLOG SUBFAMILY C MEMBER 14; 1. DR PANTHER; PTHR44665:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 14; 1. DR Pfam; PF00226; DnaJ; 1. DR Pfam; PF14901; Jiv90; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 1: Evidence at protein level; KW Chaperone; Endoplasmic reticulum; Membrane; Protein transport; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..702 FT /note="DnaJ homolog subfamily C member 14" FT /id="PRO_0000247493" FT TRANSMEM 250..270 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 300..320 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 326..346 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 443..507 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT REGION 1..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 165..229 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 658..702 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 75..84 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 88..103 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..133 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 165..175 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 192..201 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 202..217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 218..227 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..676 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 690..702 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 285 FT /note="D -> N (in Ref. 1; AAO73451)" FT /evidence="ECO:0000305" FT CONFLICT 460 FT /note="K -> R (in Ref. 1; AAO73451)" FT /evidence="ECO:0000305" SQ SEQUENCE 702 AA; 78569 MW; DAECF48B7196C7F2 CRC64; MAQKHPGERG LYGAHHSGGA SLRTLGPSVD PEIPSFSGLR DSAGTAPNGT RCLTEHSGPK HTQHPNPAHW LDPSHGPPGG PGPPRDAEDP DQSETSSEEE SGVDQELSKE NETGNQKDGN SFLSIPSACN CQGTPGIPEG PYSEGGNGSS SNFCHHCTSP ALGEDELEEE YDDEESLKFP SDFSRVSSGK KPPSRRQRHR FPTKEDTREG GRRDPRSPGR HRLGRKRSQA DKRKGLGLWG AEELCQLGQA GFWWLIELLV LVGEYVETCG HLIYACRQLK SSDLDLFRVW MGVWTGRLGG WAQVMFQFLS QGFYCGVGLF TRFLKLLGAL LLLALALFLG FLQLGWRFLV GLGDRLGWRD KATWLFSWLD SPALQRCLTL LRDSRPWQRL VRIVQWGWLE LPWVKQNINR QGNAPVASGR YCQPEEEVAR LLTMAGVPED ELNPFHVLGV EATASDVELK KAYRQLAVMV HPDKNHHPRA EEAFKVLRAA WDIVSNAEKR KEYEMKRMAE NELSRSVNEF LSKLQDDLKE AMNTMMCSRC QGKHRRFEMD REPKSARYCA ECNRLHPAEE GDFWAESSML GLKITYFALM DGKVYDITEW AGCQRVGISP DTHRVPYHIS FGSRIPGTRG RQRATPDAPP ADLQDFLSRI FQVPPGQMPN GNFFAAPQPA PGAAAASKPN STVPKGEAKP KRRKKVRRPF QR //